GSP1_YEAST - dbPTM
GSP1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GSP1_YEAST
UniProt AC P32835
Protein Name GTP-binding nuclear protein GSP1/CNR1
Gene Name GSP1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 219
Subcellular Localization Nucleus.
Protein Description GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Essential for cell viability. By analogy with Ras, Ran may be activated when GTP is exchanged for bound GDP by RCC1 and inactivated when GTP is hydrolyzed by Ran upon activation by RanGAP1..
Protein Sequence MSAPAANGEVPTFKLVLVGDGGTGKTTFVKRHLTGEFEKKYIATIGVEVHPLSFYTNFGEIKFDVWDTAGQEKFGGLRDGYYINAQCAIIMFDVTSRITYKNVPNWHRDLVRVCENIPIVLCGNKVDVKERKVKAKTITFHRKKNLQYYDISAKSNYNFEKPFLWLARKLAGNPQLEFVASPALAPPEVQVDEQLMQQYQQEMEQATALPLPDEDDADL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSAPAANGE
------CCCCCCCCC		42.8522369663
2Acetylation------MSAPAANGE
------CCCCCCCCC		42.8515665377
14UbiquitinationNGEVPTFKLVLVGDG
CCCCCEEEEEEEECC		39.9215699485
25UbiquitinationVGDGGTGKTTFVKRH
EECCCCCCCEEEEEH		44.2015699485
25SuccinylationVGDGGTGKTTFVKRH
EECCCCCCCEEEEEH		44.2023954790
25AcetylationVGDGGTGKTTFVKRH
EECCCCCCCEEEEEH		44.2024489116
252-HydroxyisobutyrylationVGDGGTGKTTFVKRH
EECCCCCCCEEEEEH		44.20-
302-HydroxyisobutyrylationTGKTTFVKRHLTGEF
CCCCEEEEEHHCCCC		29.88-
34PhosphorylationTFVKRHLTGEFEKKY
EEEEEHHCCCCEEEE		28.6527214570
39AcetylationHLTGEFEKKYIATIG
HHCCCCEEEEEEEEE		57.0822865919
392-HydroxyisobutyrylationHLTGEFEKKYIATIG
HHCCCCEEEEEEEEE		57.08-
73AcetylationWDTAGQEKFGGLRDG
EECCCCCCCCCCCCC		41.2324489116
101UbiquitinationVTSRITYKNVPNWHR
CCCCCEECCCCCHHH		42.7023749301
1012-HydroxyisobutyrylationVTSRITYKNVPNWHR
CCCCCEECCCCCHHH		42.70-
101AcetylationVTSRITYKNVPNWHR
CCCCCEECCCCCHHH		42.7024489116
125AcetylationPIVLCGNKVDVKERK
CEEECCCCCCCCCCE		25.7024489116
125UbiquitinationPIVLCGNKVDVKERK
CEEECCCCCCCCCCE		25.7023749301
129UbiquitinationCGNKVDVKERKVKAK
CCCCCCCCCCEEECE		47.5422817900
129AcetylationCGNKVDVKERKVKAK
CCCCCCCCCCEEECE		47.5424489116
1292-HydroxyisobutyrylationCGNKVDVKERKVKAK
CCCCCCCCCCEEECE		47.54-
132UbiquitinationKVDVKERKVKAKTIT
CCCCCCCEEECEEEE		49.5322817900
134UbiquitinationDVKERKVKAKTITFH
CCCCCEEECEEEEEE		47.3922817900
136UbiquitinationKERKVKAKTITFHRK
CCCEEECEEEEEEEC		34.4422817900
137PhosphorylationERKVKAKTITFHRKK
CCEEECEEEEEEECC		30.0628889911
154UbiquitinationQYYDISAKSNYNFEK
EEEEEECCCCCCCCC		32.2324961812
154AcetylationQYYDISAKSNYNFEK
EEEEEECCCCCCCCC		32.2324489116
155PhosphorylationYYDISAKSNYNFEKP
EEEEECCCCCCCCCH		44.2421440633
161AcetylationKSNYNFEKPFLWLAR
CCCCCCCCHHHHHHH		36.6124489116
181PhosphorylationPQLEFVASPALAPPE
CCEEEEECCCCCCCC		12.8528889911
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of GSP1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GSP1_YEAST !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of GSP1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MOG1_YEASTMOG1physical
11805837
GSP2_YEASTGSP2physical
11805837
YRB1_YEASTYRB1physical
11805837
RNA1_YEASTRNA1physical
11805837
IMB1_YEASTKAP95physical
11805837
AK_YEASTHOM3physical
11805837
RCC1_YEASTSRM1physical
11805837
MOG1_YEASTMOG1physical
10688190
CSE1_YEASTCSE1physical
10617640
IMB1_YEASTKAP95physical
10617640
XPOT_YEASTLOS1physical
10617640
NUP85_YEASTNUP85physical
10617640
HSP71_YEASTSSA1physical
10617640
YRB1_YEASTYRB1physical
10617640
FAR1_YEASTFAR1physical
10485850
XPOT_YEASTLOS1physical
9774653
YRB1_YEASTYRB1physical
9774653
YRB1_YEASTYRB1physical
11238397
IMB1_YEASTKAP95physical
9151683
XPO1_YEASTCRM1physical
11251069
YRB1_YEASTYRB1physical
11251069
YRB2_YEASTYRB2physical
11251069
YRB1_YEASTYRB1physical
7489726
RRP12_YEASTRRP12physical
14729571
XPO1_YEASTCRM1physical
10825193
YRB1_YEASTYRB1physical
10825193
CSE1_YEASTCSE1physical
9774694
CSE1_YEASTCSE1physical
9744791
NSP1_YEASTNSP1physical
9461539
YRB2_YEASTYRB2physical
9636166
YRB2_YEASTYRB2physical
9121474
IMB4_YEASTKAP123physical
12578832
CSE1_YEASTCSE1physical
12578832
NUP42_YEASTNUP42physical
12578832
NU159_YEASTNUP159physical
12578832
SHE1_YEASTSHE1physical
12578832
SEC3_YEASTSEC3physical
12578832
SYFA_YEASTFRS2physical
12578832
RTR1_YEASTRTR1physical
12578832
YEF3_YEASTYEL043Wphysical
12578832
MOG1_YEASTMOG1physical
12578832
RQC2_YEASTTAE2physical
12578832
YB75_YEASTYBR225Wphysical
12578832
YRB1_YEASTYRB1physical
12578832
YRB30_YEASTYRB30physical
12578832
IMB1_YEASTKAP95physical
12578832
YRB1_YEASTYRB1physical
7836422
IMB3_YEASTPSE1physical
9214382
MOG1_YEASTMOG1physical
11509570
IMB1_YEASTKAP95physical
11509570
IMB4_YEASTKAP123physical
11251069
IMB1_YEASTKAP95physical
11251069
IMB3_YEASTPSE1physical
11251069
IMB2_YEASTKAP104physical
11251069
NUP2_YEASTNUP2physical
7638224
IMB4_YEASTKAP123physical
9321403
RRP44_YEASTDIS3genetic
11404326
MOG1_YEASTMOG1genetic
9860978
MTR4_YEASTMTR4genetic
11404326
NTF2_YEASTNTF2genetic
9860978
NTF2_YEASTNTF2genetic
9199309
PDE2_YEASTPDE2genetic
9860978
RRP4_YEASTRRP4genetic
11404326
MOG1_YEASTMOG1genetic
10666614
XPO1_YEASTCRM1physical
15769879
IMB1_YEASTKAP95physical
15679097
IMB2_YEASTKAP104physical
15679097
IMB3_YEASTPSE1physical
15679097
IMB4_YEASTKAP123physical
15679097
IMB5_YEASTKAP114physical
15679097
KA120_YEASTKAP120physical
15679097
NMD5_YEASTNMD5physical
15679097
CSE1_YEASTCSE1physical
15679097
SIR4_YEASTSIR4genetic
16956377
IMB5_YEASTKAP114physical
17485461
IMB1_YEASTKAP95physical
17485461
IMB4_YEASTKAP123physical
17485461
IMB2_YEASTKAP104physical
17485461
IMB3_YEASTPSE1physical
17485461
GSP2_YEASTGSP2genetic
8455603
RAGP1_HUMANRANGAP1physical
7744835
MSN5_YEASTMSN5physical
18719252
IMB1_YEASTKAP95physical
19549784
IMA1_YEASTSRP1physical
19549784
IMB1_YEASTKAP95physical
15864302
NMD5_YEASTNMD5physical
15864302
YRB1_YEASTYRB1physical
20485264
XPO1_YEASTCRM1physical
20485264
IMB4_YEASTKAP123physical
21329658
NMD5_YEASTNMD5physical
21329658
IMB1_YEASTKAP95physical
21329658
IMB3_YEASTPSE1physical
21329658
IMB2_YEASTKAP104physical
21329658
IMB5_YEASTKAP114physical
21329658
SXM1_YEASTSXM1physical
21329658
KA120_YEASTKAP120physical
21329658
MTR10_YEASTMTR10physical
21329658
MSN5_YEASTMSN5physical
21329658
KA122_YEASTKAP122physical
21329658
YRB1_YEASTYRB1physical
21329658
CEX1_YEASTCEX1physical
22008473
XPO1_YEASTCRM1physical
23164569
IMB2_YEASTKAP104physical
25144938
RS26A_YEASTRPS26Aphysical
25144938
RS26B_YEASTRPS26Bphysical
25144938
BLM10_YEASTBLM10physical
23982732
DED1_YEASTDED1physical
26120835
XPO1_YEASTCRM1physical
26120835
SSL1_YEASTSSL1genetic
27708008
MED14_YEASTRGR1genetic
27708008
KRR1_YEASTKRR1genetic
27708008
SMD1_YEASTSMD1genetic
27708008
ARP3_YEASTARP3genetic
27708008
ERB1_YEASTERB1genetic
27708008
IMB1_YEASTKAP95physical
29146254
YRB1_YEASTYRB1physical
29146254
PHO85_YEASTPHO85physical
29146254
NTF2_HUMANNUTF2physical
27107014
NUP42_YEASTNUP42physical
28791779
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GSP1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND MASSSPECTROMETRY.

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